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RCANL_CAEEL
ID   RCANL_CAEEL             Reviewed;         207 AA.
AC   P53806; Q9U6V5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Calcipressin-like protein;
DE   AltName: Full=Down syndrome candidate region 1-like protein {ECO:0000303|PubMed:10756093};
DE   AltName: Full=Regulator of calcineurin {ECO:0000312|WormBase:F54E7.7};
GN   Name=rcan-1 {ECO:0000312|WormBase:F54E7.7};
GN   Synonyms=dscr1l {ECO:0000303|PubMed:10756093,
GN   ECO:0000312|WormBase:F54E7.7}, rcn-1 {ECO:0000303|PubMed:12684004,
GN   ECO:0000312|WormBase:F54E7.7};
GN   ORFNames=F54E7.7 {ECO:0000312|WormBase:F54E7.7};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=10756093; DOI=10.1006/geno.2000.6127;
RA   Strippoli P., Lenzi L., Petrini M., Carinci P., Zannotti M.;
RT   "A new gene family including DSCR1 (Down syndrome candidate region 1) and
RT   ZAKI-4: characterization from yeast to human and identification of DSCR1-
RT   like 2, a novel human member (DSCR1L2).";
RL   Genomics 64:252-263(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, INTERACTION WITH TAX-6, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=12684004; DOI=10.1016/s0022-2836(03)00237-7;
RA   Lee J.I., Dhakal B.K., Lee J., Bandyopadhyay J., Jeong S.Y., Eom S.H.,
RA   Kim D.H., Ahnn J.;
RT   "The Caenorhabditis elegans homologue of Down syndrome critical region 1,
RT   RCN-1, inhibits multiple functions of the phosphatase calcineurin.";
RL   J. Mol. Biol. 328:147-156(2003).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA   Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA   Shah K., Fitch D.H.;
RT   "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT   wide RNAi screen in Caenorhabditis elegans.";
RL   PLoS Genet. 7:E1002010-E1002010(2011).
RN   [5]
RP   FUNCTION, INTERACTION WITH TAX-6, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   SER-129; SER-133; 176-PRO--HIS-181 AND 201-PRO--GLN-207.
RX   PubMed=26232604; DOI=10.1016/j.jmb.2015.07.017;
RA   Li W., Bell H.W., Ahnn J., Lee S.K.;
RT   "Regulator of calcineurin (rcan-1) regulates thermotaxis behavior in
RT   Caenorhabditis elegans.";
RL   J. Mol. Biol. 427:3457-3468(2015).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=27871170; DOI=10.14348/molcells.2016.0222;
RA   Li W., Choi T.W., Ahnn J., Lee S.K.;
RT   "Allele-specific phenotype suggests a possible stimulatory activity of
RT   rcan-1 on calcineurin in Caenorhabditis elegans.";
RL   Mol. Cells 39:827-833(2016).
CC   -!- FUNCTION: Inhibits tax-6/calcineurin A phosphatase activity and thereby
CC       negatively regulates calcineurin-mediated functions (PubMed:12684004,
CC       PubMed:26232604, PubMed:27871170). Plays a role in modulating
CC       temperature-dependent calcium responses in AFD neurons and in addition,
CC       also negatively regulates thermotaxis in a tax-6-dependent manner in
CC       AFD neurons (PubMed:26232604). In response to changes in intracellular
CC       calcium levels may also regulate nuclear translocation of
CC       transcriptional regulators such as crtc-1 (PubMed:26232604). May play a
CC       role in regulating body size (PubMed:27871170). Plays a role in male
CC       tail tip morphogenesis (PubMed:21408209). {ECO:0000269|PubMed:12684004,
CC       ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:26232604,
CC       ECO:0000269|PubMed:27871170}.
CC   -!- SUBUNIT: Interacts with tax-6 (via catalytic domain); the interaction
CC       is calcium-dependent. {ECO:0000269|PubMed:12684004,
CC       ECO:0000269|PubMed:26232604}.
CC   -!- INTERACTION:
CC       P53806; Q0G819: tax-6; NbExp=5; IntAct=EBI-323055, EBI-323063;
CC   -!- TISSUE SPECIFICITY: Expressed in lateral hypodermal cells, marginal
CC       cells of the pharynx, vulva epithelial cells, ventral and dorsal nerve
CC       cords and commissures and various neurons in the anterior and posterior
CC       regions (PubMed:12684004, PubMed:27871170). Expressed in male tail
CC       structures including the diagonal muscles, sensory rays and spicules
CC       (PubMed:12684004, PubMed:27871170). Expressed in PHC neurons and most
CC       tail neurons and support cells of the phasmid neurons
CC       (PubMed:21408209). Also expressed in pharyngeal muscle, head neurons,
CC       excretory canal cells and hypodermal seam cells (PubMed:27871170).
CC       {ECO:0000269|PubMed:12684004, ECO:0000269|PubMed:21408209,
CC       ECO:0000269|PubMed:27871170}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from late embryogenesis to adulthood.
CC       {ECO:0000269|PubMed:12684004}.
CC   -!- DISRUPTION PHENOTYPE: Slightly shorter body length as compared to wild-
CC       type (PubMed:27871170). Reduced calcium responses in AFD neurons upon a
CC       temperature increase from 16 to 20 degrees Celsius as compared to wild-
CC       type (PubMed:26232604). At 17 and 20 degrees Celsius displays
CC       cryophilic behavior, preferentially migrating towards colder regions
CC       (PubMed:26232604). RNAi-mediated knockdown disrupts tail tip
CC       morphogenesis resulting in retention of the pointed larval tail tip in
CC       adult males (also known as the Lep phenotype) (PubMed:21408209).
CC       {ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:26232604,
CC       ECO:0000269|PubMed:27871170}.
CC   -!- SIMILARITY: Belongs to the RCAN family. {ECO:0000305}.
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DR   EMBL; AF176115; AAF01683.1; -; mRNA.
DR   EMBL; BX284603; CCD61769.1; -; Genomic_DNA.
DR   PIR; T34305; T34305.
DR   RefSeq; NP_498223.2; NM_065822.5.
DR   AlphaFoldDB; P53806; -.
DR   SMR; P53806; -.
DR   BioGRID; 41015; 5.
DR   IntAct; P53806; 4.
DR   STRING; 6239.F54E7.7; -.
DR   iPTMnet; P53806; -.
DR   EPD; P53806; -.
DR   PaxDb; P53806; -.
DR   PeptideAtlas; P53806; -.
DR   EnsemblMetazoa; F54E7.7.1; F54E7.7.1; WBGene00004321.
DR   GeneID; 175788; -.
DR   KEGG; cel:CELE_F54E7.7; -.
DR   UCSC; F54E7.7; c. elegans.
DR   CTD; 175788; -.
DR   WormBase; F54E7.7; CE31002; WBGene00004321; rcan-1.
DR   eggNOG; KOG4019; Eukaryota.
DR   GeneTree; ENSGT00940000170734; -.
DR   HOGENOM; CLU_076190_0_0_1; -.
DR   InParanoid; P53806; -.
DR   OMA; DMPPVVC; -.
DR   OrthoDB; 1585262at2759; -.
DR   PhylomeDB; P53806; -.
DR   PRO; PR:P53806; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00004321; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR   GO; GO:0005634; C:nucleus; ISS:WormBase.
DR   GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IPI:WormBase.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:WormBase.
DR   GO; GO:0019722; P:calcium-mediated signaling; IMP:WormBase.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:WormBase.
DR   GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR   GO; GO:0034606; P:response to hermaphrodite contact; IMP:WormBase.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:WormBase.
DR   GO; GO:0034608; P:vulval location; IMP:WormBase.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR006931; Calcipressin.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR10300; PTHR10300; 1.
DR   Pfam; PF04847; Calcipressin; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..207
FT                   /note="Calcipressin-like protein"
FT                   /id="PRO_0000211423"
FT   REGION          176..181
FT                   /note="Required for tax-6 interaction"
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   SITE            129
FT                   /note="May be required for inhibiting calcineurin activity"
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   SITE            133
FT                   /note="May be required for inhibiting calcineurin activity"
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   MUTAGEN         129
FT                   /note="S->A: Resistant to serotonin-induced egg laying, a
FT                   behavior positively regulated by calcineurin activity,
FT                   resulting in a reduced number of eggs laid in a tax-6
FT                   (jh107) gain-of-function mutant background."
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   MUTAGEN         133
FT                   /note="S->A: Resistant to serotonin-induced egg laying, a
FT                   behavior positively regulated by calcineurin activity,
FT                   resulting in a reduced number of eggs laid in a tax-6
FT                   (jh107) gain-of-function mutant background."
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   MUTAGEN         176..181
FT                   /note="Missing: Abolished interaction with tax-6 in a yeast
FT                   two-hybrid assay."
FT                   /evidence="ECO:0000269|PubMed:26232604"
FT   MUTAGEN         201..207
FT                   /note="Missing: Reduced body size as compared to wild-
FT                   type."
FT                   /evidence="ECO:0000269|PubMed:26232604"
SQ   SEQUENCE   207 AA;  23030 MW;  0154E308AB0D5B79 CRC64;
     MVADNSEKST KSVANGSLIS TVSSKDDLPN AIIVTQVPED VFDNKQDKAN FSSLFTQIEK
     DIHFDFLRSF RRVRVIFSSP ENATAAKLIV QGFSFKGHEL KAFFAQRIYM SANSQMLSPP
     PLEKQFLISP PCSPPVGWEQ TKDMPPVVCN FDLMARLASF AIDEKYEVHN GDELTPAIIV
     HPCETPIDVP SAIEMPRTPR PSSPCEQ
 
 
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